BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
9th Edition
ISBN: 9781319425746
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 2, Problem 37P
Interpretation Introduction
Interpretation:
The meaning of the statement referring post translational modifications as “Nature’s escape from genetic imprisonment” should be explained.
Concept introduction:
Post-translational modifications are mechanisms which amino acid residues in a protein are covalently modified after protein biosynthesis. For example, phosphorylation is most common post translational modification. Glycosylation and lipidation are also post translational modifications. Proteins are modified by modifying existing
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Briefly describe each of the following possible posttranslational protein modifications. Give an example of each.
Cross-linkage
glycosylation and phosphorylation
cleavage
assembly into polymeric proteins (> 1 polypeptide)
A- what are the Genetic Pathways of organisms? Draw a general of it.
B- define the term posttranslational modification. Why they are important?
Explain Posttranslational modification of proteins?
Chapter 2 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Post-translational modification of proteins refers to the covalent and enzymatic modification of proteins following protein biosynthesis. Give three (3) examples and briefly describe why the modification is important.arrow_forwardWhat enzyme catalyzes protein synthesis in bacteria? You discover a new broad-spectrum antibiotic that inhibits protein synthesis and named it Compound J. You want to determine the mechanism of action of Compound J. After treating bacteria cells with Compound J, you observe many ribosomes with long polypeptide chains bound to them. Based on this observation, make a hypothesis about which part of the ribosome Compound J is binding and how this specifically affects translation. What evidence supports that proper protein folding is essential to all domains of life? Name and describe the function/s of two specific molecules that help proteins fold in bacteria.arrow_forwardIn posttranslational modification, phosphates are attached to which 3 amino acids? - tyrosine - serine - proline - lysine - threoninearrow_forward
- . The genetic code is thought to have evolved to maximize genetic stability by minimizing the effect on protein function of most substitution muta- tions (single-base changes). We will use the six arginine codons to test this idea. Consider all of the substitutions that could affect all of the six arginine codons. (a) How many total mutations are possible? (b) How many of these mutations are "silent," in the sense that the mutant codon is changed to another Arg codon? (c) How many of these mutations are conservative, in the sense that an Arg codon is changed to a functionally similar Lys codon?arrow_forwardWhich would have the most serious effect on polypeptide product?arrow_forwardWhy might it be advantageous to add a preassembled block of 14 sugar residues to a protein in the er, rather than building the sugar chains step-by-step on the surface of the protein by the sequential addition of sugars by individual enzymes?arrow_forward
- The genetic code is thought to have evolved to maximize genetic stability by minimizing the effect on protein function of most substitution mutations (single-base changes). We will use the six arginine codons to test this idea. Consider all of the substitutions that could affect all of the six arginine codons.(a) How many total mutations are possible?(b) How many of these mutations are “silent,” in the sense that the mutantcodon is changed to another Arg codon?(c) How many of these mutations are conservative, in the sense that an Argcodon is changed to a functionally similar Lys codon?arrow_forwardHydrogen bonds are important in DNA replication and transcription. They are relatively weak chemical bonds. Why is this a desirable feature for DNA? Describe the effect (s) of changing (mutating) the promoter on the transcription of the DNA strand/gene the promoter controls. What happens to protein synthesis if a nonsense codon is inserted into the gene? Explain why a point mutation does not necessarily change the original amino acid sequence. (Explain silent mutations) Choose any pentapeptide composed of five different amino acids. List the amino acids. Present one messenger RNA codon for each amino acids and the sequence of nucleotides on the DNA that originally coded for your pentapeptide.arrow_forwardWhen glycoproteins are synthesized in the cell, at what stage of the polymerization of the protein are the sugar groups added: Prior to translation, cotranslationally, or posttranslationally?arrow_forward
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